Literature summary for 3.4.16.4 extracted from

Silvaggi, N.R.; Josephine, H.R.; Kuzin, A.P.; Nagarajan, R.; Pratt, R.F.; Kelly, J.A.
Crystal structures of complexes between the R61 DD-peptidase and peptidoglycan-mimetic beta-lactams: a non-covalent complex with a "perfect penicillin" (2005), J. Mol. Biol., 345, 521-533.

Search for more literature for 3.4.16.4

Application

Application	Comment	Organism
medicine	clinical defense against bacterial infections, DD-peptidases are the killing targets of beta-lactams	Streptomyces sp. R61

Crystallization (Commentary)

Crystallization (Comment)	Organism
by hanging-drop, vapor-diffusion method, to 1.5 A resolution, X-ray structure of non-covalent and covalent complexes of beta-lactams with DD-peptidase	Streptomyces sp. R61

Inhibitors

Inhibitors	Comment	Organism	Structure
benzylpenicillin	classical non-specific beta-lactam	Streptomyces sp. R61
cephalosporin	with glycyl-L-alpha-amino-epsilon-pimelyl side-chain, this beta lactam might be a better antibiotic than a non-specific counterpart	Streptomyces sp. R61
cephalosporin C	classical non-specific beta-lactam	Streptomyces sp. R61
penicillin	having the glycyl-L-alpha-amino-epsilon-pimelyl side-chain of Streptomyces strain R61 peptidoglycan, this beta lactam might be the perfect antibiotic as compared to a non-specific counterpart	Streptomyces sp. R61

Organism

Organism	UniProt	Comment	Textmining
Streptomyces sp. R61	P15555	-	-

Synonyms

Synonyms	Comment	Organism
D-alanyl-D-alanine-transpeptidase	-	Streptomyces sp. R61
DD-peptidase	-	Streptomyces sp. R61

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Release 2023.1 (January 2023)